Isolation of a stable enzyme.14CO2.Mg2+.carboxyarabinitol bisphosphate complex with ribulosebisphosphate carboxylase from Chromatium vinosum.
Higher plant-type ribulosebisphoshate carboxylase from Chromatium vinosum formed a stable, nonexchangeable complex with activator 14CO2 in the presence of Mg2+ and 2-carboxyarabinitol bisphosphate, an analog of the proposed transition-state intermediate. The response of the procaryotic enzyme to this analog was indistinguishable from that of the higher-plant carboxylase, which should permit comparative analysis of the activator site amino acid sequence in the two proteins.
D001665:Binding Sites; D002245:Carbon Dioxide / Q000378:metabolism*; D002262:Carboxy-Lyases / Q000378:metabolism*; D055598:Chemical Phenomena; D002621:Chemistry; D002844:Chromatium / Q000201:enzymology*; D004789:Enzyme Activation; D008274:Magnesium / Q000378:metabolism*; D010428:Pentosephosphates; D012273:Ribulose-Bisphosphate Carboxylase / Q000378:metabolism*; D013402:Sugar Alcohols; D013403:Sugar Phosphates / Q000378:metabolism*
D010428:Pentosephosphates; D013402:Sugar Alcohols; D013403:Sugar Phosphates; D002245:Carbon Dioxide; C032687:2-carboxyarabinitol 1,5-biphosphate; D002262:Carboxy-Lyases; D012273:Ribulose-Bisphosphate Carboxylase; D008274:Magnesium